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Volumn 141, Issue 4, 2013, Pages 3435-3442

Extraction of antioxidative and antihypertensive bioactive peptides from Parkia speciosa seeds

Author keywords

Antihypertensive; Antioxidative; Bioactive peptide; Parkia speciosa

Indexed keywords

ANTIOXIDANTS; ENZYMES; TEMPERATURE;

EID: 84884579645     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2013.06.030     Document Type: Article
Times cited : (115)

References (29)
  • 2
    • 33748565005 scopus 로고    scopus 로고
    • α-Amylase inhibitory activity of some Malaysian plants used to treat diabetes; With particular reference to Phyllanthus amarus
    • DOI 10.1016/j.jep.2006.04.004, PII S0378874106001863
    • Ali, H., Houghton, P. J., & Soumyanath, A. (2006). a-Amylase inhibitory activity of some Malaysian plants used to treat diabetes; with particular reference to Phyllanthus amarus. Journal of Ethnopharmacology, 107, 449-455 (Pubitemid 44363032)
    • (2006) Journal of Ethnopharmacology , vol.107 , Issue.3 , pp. 449-455
    • Ali, H.1    Houghton, P.J.2    Soumyanath, A.3
  • 3
    • 79960845541 scopus 로고    scopus 로고
    • Effects of enzymatic hydrolysis on molecular structure and antioxidant activity of barley hordein
    • Bamdad, F., Wu, J., & Chen, L. (2011). Effects of enzymatic hydrolysis on molecular structure and antioxidant activity of barley hordein. Journal of Cereal Science, 54, 20-28
    • (2011) Journal of Cereal Science , vol.54 , pp. 20-28
    • Bamdad, F.1    Wu, J.2    Chen, L.3
  • 4
    • 0030586361 scopus 로고    scopus 로고
    • The ferric reducing ability of plasma (FRAP) as a measure of "antioxidant power": The FRAP Assay
    • Benzie, I. F. F., & Strain, J. J. (1996). The ferric reducing ability of plasma (FRAP) as a measure of "antioxidant power": The FRAP Assay. Analytical Biochemistry, 239, 70-76
    • (1996) Analytical Biochemistry , vol.239 , pp. 70-76
    • Benzie, I.F.F.1    Strain, J.J.2
  • 6
    • 0019332139 scopus 로고
    • Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence
    • Cheung, H. S., Wang, F. L., Ondetti, M. A., Sabo, E. F., & Cushman, D. W. (1980). Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence. Journal of Biological Chemistry, 255, 401-407
    • (1980) Journal of Biological Chemistry , vol.255 , pp. 401-407
    • Cheung, H.S.1    Wang, F.L.2    Ondetti, M.A.3    Sabo, E.F.4    Cushman, D.W.5
  • 7
    • 0015083353 scopus 로고
    • Spectrophotometric assay and properties of the angiotensin-converting enzyme of rabbit lung
    • Cushman, D. W., & Cheung, H. S. (1971). Spectrophotometric assay and properties of the angiotensin-converting enzyme of rabbit lung. Biochemical Pharmacology, 20, 1637-1648
    • (1971) Biochemical Pharmacology , vol.20 , pp. 1637-1648
    • Cushman, D.W.1    Cheung, H.S.2
  • 8
    • 32344435383 scopus 로고    scopus 로고
    • Grain legume proteins and nutraceutical properties
    • DOI 10.1016/j.fitote.2005.11.008, PII S0367326X0500239X
    • Duranti, M. (2006). Grain legume proteins and nutraceutical properties. Fitoterapia, 77, 67-82 (Pubitemid 43220250)
    • (2006) Fitoterapia , vol.77 , Issue.2 , pp. 67-82
    • Duranti, M.1
  • 9
    • 34147123803 scopus 로고    scopus 로고
    • Food-derived peptides with biological activity: From research to food applications
    • DOI 10.1016/j.copbio.2007.01.013, PII S0958166907000146, Plant Biotechnology / Food Biotechnology
    • Hartmann, R., & Meisel, H. (2007). Food-derived peptides with biological activity: From research to food applications. Current Opinion in Biotechnology, 18, 163-169 (Pubitemid 46575225)
    • (2007) Current Opinion in Biotechnology , vol.18 , Issue.2 , pp. 163-169
    • Hartmann, R.1    Meisel, H.2
  • 10
    • 34548243982 scopus 로고    scopus 로고
    • High throughput and rapid screening of marine protein hydrolysates enriched in peptides with angiotensin-I-converting enzyme inhibitory activity by capillary electrophoresis
    • DOI 10.1016/j.biortech.2006.11.036, PII S0960852406006122
    • He, H. L., Chen, X. L., Wu, H., Sun, C. Y., Zhang, Y. Z., & Zhou, B. C. (2007). High throughput and rapid screening of marine protein hydrolysates enriched in peptides with angiotensin-I-converting enzyme inhibitory activity by capillary electrophoresis. Bioresource Technology, 98, 3499-3505 (Pubitemid 47333129)
    • (2007) Bioresource Technology , vol.98 , Issue.18 , pp. 3499-3505
    • He, H.-L.1    Chen, X.-L.2    Wu, H.3    Sun, C.-Y.4    Zhang, Y.-Z.5    Zhou, B.-C.6
  • 11
    • 59849087348 scopus 로고    scopus 로고
    • Effects of thermal treatment on the coagulation of soy proteins induced by subtilisin Carlsberg
    • Inouye, K., Nakano, K., Asaoka, K., & Yasukawa, K. (2009). Effects of thermal treatment on the coagulation of soy proteins induced by subtilisin Carlsberg. Journal of Agricultural and Food Chemistry, 57, 717-723
    • (2009) Journal of Agricultural and Food Chemistry , vol.57 , pp. 717-723
    • Inouye, K.1    Nakano, K.2    Asaoka, K.3    Yasukawa, K.4
  • 12
  • 13
    • 0034840775 scopus 로고    scopus 로고
    • Angiotensin I converting enzyme inhibitory peptides purified from bovine skin gelatin hydrolysate
    • Kim, S. K., Byun, H. G., Park, P. J., & Shahidi, F. (2001). Angiotensin I converting enzyme inhibitory peptides purified from bovine skin gelatin hydrolysate. Journal of Agricultural and Food Chemistry, 49, 2992-2997 (Pubitemid 32826100)
    • (2001) Journal of Agricultural and Food Chemistry , vol.49 , Issue.6 , pp. 2992-2997
    • Kim, S.-K.1    Byun, H.-G.2    Park, P.-J.3    Shahidi, F.4
  • 14
    • 33747503962 scopus 로고    scopus 로고
    • Bioactive peptides: Production and functionality
    • DOI 10.1016/j.idairyj.2005.10.012, PII S0958694605002426
    • Korhonen, H., & Pihlanto, A. (2006). Bioactive peptides: Production and functionality. International Dairy Journal, 16, 945-960 (Pubitemid 44255683)
    • (2006) International Dairy Journal , vol.16 , Issue.9 , pp. 945-960
    • Korhonen, H.1    Pihlanto, A.2
  • 15
    • 0027142694 scopus 로고
    • Action of transglutaminase on the constitutive polypeptides of pea legumin
    • Larré, C., Chiarello, M., Dudek, S., Chenu, M., & Gueguen, J. (1993). Action of transglutaminase on the constitutive polypeptides of pea legumin. Journal of Agriculture and Food Chemistry, 41, 1816-1820 (Pubitemid 2006978)
    • (1993) J. Agric. Food Chem. , vol.41 , Issue.11 , pp. 1816-1820
    • Larre, C.1    Chiarello, M.2    Dudek, S.3    Chenu, M.4    Gueguen, J.5
  • 16
    • 0000793859 scopus 로고    scopus 로고
    • Purification and identification of angiotensin-I converting enzyme inhibitory peptide form kidney bean protein hydrolysate
    • Lee, J. R., Kwon, D. Y., Shin, H. K., & Yang, C. B. (1999). Purification and identification of angiotensin-I converting enzyme inhibitory peptide form kidney bean protein hydrolysate. Food Science and Biotechnology, 8, 172-178
    • (1999) Food Science and Biotechnology , vol.8 , pp. 172-178
    • Lee, J.R.1    Kwon, D.Y.2    Shin, H.K.3    Yang, C.B.4
  • 17
    • 84866168471 scopus 로고    scopus 로고
    • Improving antioxidant activities of whey protein hydrolysates obtained by thermal preheat treatment of pepsin, trypsin, alcalase and flavourzyme
    • Lin, S., Tian, W., Li, H., Cao, J., & Jiang, W. (2012). Improving antioxidant activities of whey protein hydrolysates obtained by thermal preheat treatment of pepsin, trypsin, alcalase and flavourzyme. International Journal of Food Science & Technology, 47, 2045-2051
    • (2012) International Journal of Food Science & Technology , vol.47 , pp. 2045-2051
    • Lin, S.1    Tian, W.2    Li, H.3    Cao, J.4    Jiang, W.5
  • 18
    • 0001524478 scopus 로고
    • On the determination of cystine as cysteic acid
    • Moore, S. (1963). On the determination of cystine as cysteic acid. The Journal of Biological Chemistry, 238, 235-237
    • (1963) The Journal of Biological Chemistry , vol.238 , pp. 235-237
    • Moore, S.1
  • 19
    • 0024215260 scopus 로고
    • Protective role of sulfhydryl reagents in oxidant lung injury
    • Patterson, C. E., & Rhoades, R. A. (1988). Protective role of sulfhydryl reagents in oxidant lung injury. Experimental Lung Research, 14, 1005-1019 (Pubitemid 19016173)
    • (1988) Experimental Lung Research , vol.14 , Issue.SUPPL. , pp. 1005-1019
    • Patterson, C.E.1    Rhoades, R.A.2
  • 20
    • 10044257367 scopus 로고    scopus 로고
    • Thermal heat processing effects on antinutrients, protein and starch digestibility of food legumes
    • DOI 10.1016/j.foodchem.2004.06.019, PII S0308814604004649
    • Rehman, Z. U., & Shah, W. H. (2005). Thermal heat processing effects on antinutrients, protein and starch digestibility of food legumes. Food Chemistry, 91, 327-331 (Pubitemid 39601646)
    • (2005) Food Chemistry , vol.91 , Issue.2 , pp. 327-331
    • Rehman, Z.-U.1    Shah, W.H.2
  • 21
    • 80052966203 scopus 로고    scopus 로고
    • Antibacterial activity of Thai edible plants against gastrointestinal pathogenic bacteria and isolation of a new broad spectrum antibacterial polyisoprenylated benzophenone, chamuangone
    • Sakunpak, A., & Panichayupakaranant, P. (2012). Antibacterial activity of Thai edible plants against gastrointestinal pathogenic bacteria and isolation of a new broad spectrum antibacterial polyisoprenylated benzophenone, chamuangone. Food Chemistry, 130, 826-831
    • (2012) Food Chemistry , vol.130 , pp. 826-831
    • Sakunpak, A.1    Panichayupakaranant, P.2
  • 22
    • 19044365083 scopus 로고    scopus 로고
    • The classification, functions and evolutionary relationships of plant proteins in relation to food allergies
    • E. N. Clare Mills & P. R. Shewry (Eds.) Oxford, UK: Blackwell Science
    • Shewry, P. R., Jenkins, J. A., Beaudoin, F., & Clara Mills, E. N. (2004). The classification, functions and evolutionary relationships of plant proteins in relation to food allergies. In E. N. Clare Mills & P. R. Shewry (Eds.), Plant food allergens (pp. 24-41). Oxford, UK: Blackwell Science.
    • (2004) Plant Food Allergens , pp. 24-41
    • Shewry, P.R.1    Jenkins, J.A.2    Beaudoin, F.3    Clara Mills, E.N.4
  • 24
    • 60249084349 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of hemp (Cannabis sativa L.) protein isolate by various proteases and antioxidant properties of the resulting hydrolysates
    • Tang, C. H., Wang, X. S., & Yang, X. Q. (2009). Enzymatic hydrolysis of hemp (Cannabis sativa L.) protein isolate by various proteases and antioxidant properties of the resulting hydrolysates. Food Chemistry, 114, 1484-1490
    • (2009) Food Chemistry , vol.114 , pp. 1484-1490
    • Tang, C.H.1    Wang, X.S.2    Yang, X.Q.3
  • 26
    • 79957795842 scopus 로고    scopus 로고
    • Chemometric analysis of the amino acid requirements of antioxidant food protein hydrolysates
    • Udenigwe, C. C., & Aluko R. E. (2011). Chemometric analysis of the amino acid requirements of antioxidant food protein hydrolysates. International Journal of Molecular Sciences, 12, 3148-3161
    • (2011) International Journal of Molecular Sciences , vol.12 , pp. 3148-3161
    • Udenigwe, C.C.1    Aluko, R.E.2
  • 27
    • 84856032752 scopus 로고    scopus 로고
    • Food protein-derived bioactive peptides: Production, procesing, and potential health benefits
    • Udenigwe, C. C., & Aluko, R. E. (2012). Food protein-derived bioactive peptides: Production, procesing, and potential health benefits. Journal of Food Science, 77, R11-R24
    • (2012) Journal of Food Science , vol.77
    • Udenigwe, C.C.1    Aluko, R.E.2
  • 28
    • 33750942072 scopus 로고    scopus 로고
    • Assessment of the protein quality of fourteen soybean [Glycine max (L.) Merr.] cultivars using amino acid analysis and two-dimensional electrophoresis
    • DOI 10.1016/j.foodres.2006.08.006, PII S0963996906001311
    • Zarkadas, C. G., Gagnon, C., Gleddie, S., Khanizadeh, S., Cober, E. R., & Guillemette, R. J. D. (2007). Assessment of the protein quality of fourteen soybean [Glycine max (L.) Merr.] cultivars using amino acid analysis and two-dimensional electrophoresis. Food Research International, 40, 129-146 (Pubitemid 44738540)
    • (2007) Food Research International , vol.40 , Issue.1 , pp. 129-146
    • Zarkadas, C.G.1    Gagnon, C.2    Gleddie, S.3    Khanizadeh, S.4    Cober, E.R.5    Guillemette, R.J.D.6
  • 29
    • 36048952787 scopus 로고    scopus 로고
    • Antihypertensive effect and purification of an ACE inhibitory peptide from sea cucumber gelatin hydrolysate
    • DOI 10.1016/j.procbio.2007.08.011, PII S1359511307002346
    • Zhao, Y., Li, B., Liu, Z., Dong, S., Zhao, X., & Zeng, M. (2007). Antihypertensive effect and purification of an ACE inhibitory peptide from sea cucumber gelatin hydrolysate. Process Biochemistry, 42, 1586-1591 (Pubitemid 350101340)
    • (2007) Process Biochemistry , vol.42 , Issue.12 , pp. 1586-1591
    • Zhao, Y.1    Li, B.2    Liu, Z.3    Dong, S.4    Zhao, X.5    Zeng, M.6


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